Abstract
The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity.
MeSH terms
-
Epigenesis, Genetic*
-
Histones / chemistry
-
Histones / metabolism*
-
Lysine / analogs & derivatives*
-
Lysine / chemistry
-
Lysine / metabolism*
-
Models, Molecular
-
Molecular Structure
-
Protein Domains
-
Protein Processing, Post-Translational*
-
Saccharomyces cerevisiae / metabolism*
-
Saccharomyces cerevisiae Proteins / chemistry*
-
Saccharomyces cerevisiae Proteins / metabolism*
-
Transcription Factor TFIID / chemistry*
-
Transcription Factor TFIID / metabolism*
Substances
-
Histones
-
Saccharomyces cerevisiae Proteins
-
TAF14 protein, S cerevisiae
-
Transcription Factor TFIID
-
Lysine